Dielectric measurements of lysozyme and tri-N-acetyl-D-glucosamine association at radio and microwave frequencies.
Time domain dielectric measurements were applied to the monitoring of molecular recognition by proteins. Lysozyme and tri-N-acetyl-D-glucosamine((NAG)3) were selected as a typical lock and key type recognition system. After association of (NAG)3, relaxation related to lysozyme itself was increased and depended on the pH of the solution. No change was detected in hydration of the enzyme before and after association.
Amo
Y
Y
Research Center for Advanced Science and Technology, University of Tokyo, Japan.
Karube
I
I
D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D008872:Microwaves; D009113:Muramidase / Q000032:analysis*; D011846:Radio Waves; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014312:Trisaccharides / Q000032:analysis*
D014312:Trisaccharides; C019117:N,N',N''-triacetylchitotriose; D009113:Muramidase